Evidence map›Paper›PMID 36525666›Full record

ArticleACS chemical biology2023

Engineered Glycan-Binding Proteins for Recognition of the Thomsen-Friedenreich Antigen and Structurally Related Disaccharides.

Elizabeth M Ward, Cristina Y Zamora, Nathaniel S Schocker, Soumi Ghosh, Megan E Kizer, Barbara Imperiali

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 9 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Elizabeth M WardDepartment of Biology, Massachusetts Institute of Technology, 31 Ames St, Cambridge, Massachusetts 02142, United States.ORCID 0000-0001-6410-1116
Cristina Y ZamoraDepartment of Biology, Massachusetts Institute of Technology, 31 Ames St, Cambridge, Massachusetts 02142, United States.ORCID 0000-0002-7241-6713
Nathaniel S SchockerDepartment of Biology, Massachusetts Institute of Technology, 31 Ames St, Cambridge, Massachusetts 02142, United States.
Soumi GhoshDepartment of Biology, Massachusetts Institute of Technology, 31 Ames St, Cambridge, Massachusetts 02142, United States.ORCID 0000-0001-6101-0147
Megan E KizerDepartment of Biology, Massachusetts Institute of Technology, 31 Ames St, Cambridge, Massachusetts 02142, United States.ORCID 0000-0003-3549-8606
Barbara ImperialiDepartment of Biology, Massachusetts Institute of Technology, 31 Ames St, Cambridge, Massachusetts 02142, United States.ORCID 0000-0002-5749-7869
Massachusetts Institute of Technology · US

Funding

Interdepartmental Biotechnology Training ProgramT32GM008334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WITTRUP, KARL DANE · 1989 to 2018
$15.2M
Development of multifunctional probes for profiling microbial glycansU01CA231079 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI IMPERIALI, BARBARA, KIESSLING, LAURA L · 2018 to 2020
$1.4M
NCI NIH HHS U01 CA231079NIGMS NIH HHS T32 GM008334
6 · The paper itself

Abstract

Glycan-binding proteins (GBPs) are widely used reagents for basic research and clinical applications. These reagents allow for the identification and manipulation of glycan determinants without specialized equipment or time-consuming experimental methods. Existing GBPs, mainly antibodies and lectins, are limited, and discovery or creation of reagents with novel specificities is time consuming and difficult. Here, we detail the generation of GBPs from a small, hyper-thermostable DNA-binding protein by directed evolution. Yeast surface display of a variable library of rcSso7d proteins was screened to find variants with selectivity toward the cancer-associated glycan Galβ1-3GalNAcα or Thomsen-Friedenreich antigen and various relevant disaccharides. Characterization of these proteins shows them to have specificities and affinities on par with currently available lectins. The proteins can be readily functionalized with fluorophores or biotin using sortase-mediated ligation to create reagents that prove useful for glycoprotein blotting and cell staining applications. The presented methods for the development of GBPs toward specific saccharides of interest will have great impact on both biomedical and glycobiological research.

Indexed as

Carrier ProteinsDisaccharidesAntigens, Tumor-Associated, CarbohydrateLectinsAntigens, Tumor-Associated, CarbohydrateCarrier ProteinsDisaccharidesLectinsThomsen-Friedenreich antigen

Identifiers

PMID36525666
PMCPMC9868099
OpenAlexW4311824625

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.